Worm Breeder's Gazette 3(2): 21a
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
My most recent efforts have involved the purification and characterization of a major protein component found in purified sperm with my major objective being to investigate a developmentally regulated gene at both the cellular and molecular level. This sperm protein is first synthesized around 76 hours after hatching (16 C time) as determined by pulse-labeling males during different developmental stages. The synthesis of this protein has a molecular weight of 14, 000 in SDS gels, an isoelectric point between 8.6 and 8.8 and accounts for approximately 20% of the total protein found in isolated sperm. Although the protein shows a molecular weight of 14,000 under denaturing conditions, it shows a molecular weight of 28,000 when using Sephadex or Bio-gel in nondenaturing conditions. The protein can be purified by homogenizing sperm and running the S100 over a phosphocellulose column. This basic protein is the only protein in the S100 that binds to phosphocellulose. I am using this purified protein preparation to obtain specific antibodies and will use the antibody to determine the structural significance of this protein by EM immunological techniques. The adult male contains a significant amount of polyA containing mRNA that codes for this basic sperm protein as determined in a recticulocyte translation system. I am now in the process of purifying this specific mRNA. By using 35S-sufanilic acid diazonium salt it does not appear that this protein is a cell surface protein but seems to be contained within the cell.